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Protein

Serine/threonine-protein kinase SKY1

Gene

SKY1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Constitutively active kinase, specifically and sequentially phosphorylates serine/arginine (SR)-type shuttling mRNA binding proteins in their RS dipeptide repeats.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei187 – 1871ATPPROSITE-ProRule annotation
Active sitei294 – 2941Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi164 – 1729ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protein serine/threonine kinase activity Source: SGD

GO - Biological processi

  • cellular cation homeostasis Source: SGD
  • cellular ion homeostasis Source: SGD
  • mRNA splice site selection Source: SGD
  • positive regulation of protein import into nucleus Source: SGD
  • protein phosphorylation Source: SGD
  • response to drug Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-32899-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase SKY1 (EC:2.7.11.1)
Short name:
SRPK
Gene namesi
Name:SKY1
Ordered Locus Names:YMR216C
ORF Names:YM8261.10C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YMR216C.
SGDiS000004829. SKY1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 742742Serine/threonine-protein kinase SKY1PRO_0000086658Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei383 – 3831PhosphothreonineCombined sources
Modified residuei386 – 3861PhosphothreonineCombined sources
Modified residuei388 – 3881PhosphoserineCombined sources
Modified residuei393 – 3931PhosphoserineCombined sources
Modified residuei410 – 4101PhosphoserineCombined sources
Modified residuei427 – 4271PhosphoserineCombined sources
Modified residuei432 – 4321PhosphoserineCombined sources
Modified residuei445 – 4451PhosphoserineCombined sources
Modified residuei449 – 4491PhosphoserineCombined sources
Modified residuei453 – 4531PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ03656.
PeptideAtlasiQ03656.

PTM databases

iPTMnetiQ03656.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
TOR1P351692EBI-9800,EBI-19374

Protein-protein interaction databases

BioGridi35394. 243 interactions.
DIPiDIP-2884N.
IntActiQ03656. 16 interactions.
MINTiMINT-1738833.

Structurei

Secondary structure

1
742
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni154 – 1574Combined sources
Beta strandi158 – 1669Combined sources
Beta strandi168 – 17710Combined sources
Turni178 – 1814Combined sources
Beta strandi182 – 1898Combined sources
Helixi193 – 21119Combined sources
Helixi216 – 2227Combined sources
Beta strandi230 – 2367Combined sources
Beta strandi239 – 2468Combined sources
Helixi253 – 2597Combined sources
Turni260 – 2623Combined sources
Helixi267 – 28620Combined sources
Helixi297 – 2993Combined sources
Beta strandi300 – 3045Combined sources
Turni539 – 5424Combined sources
Beta strandi543 – 5486Combined sources
Helixi551 – 5533Combined sources
Helixi568 – 5703Combined sources
Helixi573 – 5775Combined sources
Helixi584 – 59916Combined sources
Beta strandi610 – 6123Combined sources
Helixi615 – 62612Combined sources
Helixi631 – 6366Combined sources
Helixi640 – 6434Combined sources
Beta strandi650 – 6523Combined sources
Helixi661 – 6677Combined sources
Helixi673 – 68311Combined sources
Helixi684 – 6874Combined sources
Turni691 – 6933Combined sources
Helixi697 – 7015Combined sources
Helixi704 – 7063Combined sources
Turni710 – 7145Combined sources
Helixi726 – 7283Combined sources
Beta strandi732 – 7343Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HOWX-ray2.10A138-304[»]
A539-742[»]
1Q8YX-ray2.05A/B138-304[»]
A/B539-742[»]
1Q8ZX-ray2.35A/B138-304[»]
A/B539-742[»]
1Q97X-ray2.30A/B138-304[»]
A/B539-742[»]
1Q99X-ray2.11A/B138-304[»]
A/B539-742[»]
2JD5X-ray2.50A/B138-742[»]
ProteinModelPortaliQ03656.
SMRiQ03656. Positions 142-313, 537-737.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ03656.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini158 – 706549Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00530000063566.
HOGENOMiHOG000171558.
InParanoidiQ03656.
KOiK08832.
OMAiDASISCE.
OrthoDBiEOG7SV148.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 2 hits.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q03656-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSSINYPGF VTKSAHLADT STDASISCEE ATSSQEAKKN FFQRDYNMMK
60 70 80 90 100
KAPAPTKSKL SLALQTSKSS SSANGTVQED TSSKTEDFST KSIKKKPDSG
110 120 130 140 150
VESHVSIQSD SGPQSDSDLD SDSSISSCDE RNEESLKDYR PGGYHPAFKG
160 170 180 190 200
EPYKDARYIL VRKLGWGHFS TVWLAKDMVN NTHVAMKIVR GDKVYTEAAE
210 220 230 240 250
DEIKLLQRVN DADNTKEDSM GANHILKLLD HFNHKGPNGV HVVMVFEVLG
260 270 280 290 300
ENLLALIKKY EHRGIPLIYV KQISKQLLLG LDYMHRRCGI IHTDIKPENV
310 320 330 340 350
LMEIGDVEGI VQMVEALDKQ KREAKRLQRH VSRSSDITAN DSSDEKWAEC
360 370 380 390 400
QTSMPCGSSS NSKSRSIEKD LSKRCFRRPR RHTIITGSQP LPSPISSSNF
410 420 430 440 450
FEMRAHFCGS SHNSFSSVSG NRNIPSSINN NSINNGIGIK NSNNSFLNSV
460 470 480 490 500
PHSVTRMFIN EDSNDNNNND NSKNKNNNNN NSNNNNNEDI MNTPLHEEQL
510 520 530 540 550
ADSLSTFDIS NISQSSDTNG PYISNTMDSN SNVSTDINSP ENLIQIKIAD
560 570 580 590 600
LGNACWYDEH YTNSIQTREY RSPEVLLGAP WGCGADIWST ACLIFELITG
610 620 630 640 650
DFLFEPDEGH SYTKDDDHIA QIIELLGELP SYLLRNGKYT RTFFNSRGLL
660 670 680 690 700
RNISKLKFWP LEDVLTEKYK FSKDEAKEIS DFLSPMLQLD PRKRADAGGL
710 720 730 740
VNHPWLKDTL GMEEIRVPDR ELYGSGSDIP GWFEEVRDHK RH
Length:742
Mass (Da):83,238
Last modified:November 1, 1997 - v1
Checksum:iC775F10B30C950FC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49809 Genomic DNA. Translation: CAA89931.1.
BK006946 Genomic DNA. Translation: DAA10115.1.
PIRiS55098.
RefSeqiNP_013943.1. NM_001182723.1.

Genome annotation databases

EnsemblFungiiYMR216C; YMR216C; YMR216C.
GeneIDi855256.
KEGGisce:YMR216C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49809 Genomic DNA. Translation: CAA89931.1.
BK006946 Genomic DNA. Translation: DAA10115.1.
PIRiS55098.
RefSeqiNP_013943.1. NM_001182723.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HOWX-ray2.10A138-304[»]
A539-742[»]
1Q8YX-ray2.05A/B138-304[»]
A/B539-742[»]
1Q8ZX-ray2.35A/B138-304[»]
A/B539-742[»]
1Q97X-ray2.30A/B138-304[»]
A/B539-742[»]
1Q99X-ray2.11A/B138-304[»]
A/B539-742[»]
2JD5X-ray2.50A/B138-742[»]
ProteinModelPortaliQ03656.
SMRiQ03656. Positions 142-313, 537-737.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35394. 243 interactions.
DIPiDIP-2884N.
IntActiQ03656. 16 interactions.
MINTiMINT-1738833.

PTM databases

iPTMnetiQ03656.

Proteomic databases

MaxQBiQ03656.
PeptideAtlasiQ03656.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR216C; YMR216C; YMR216C.
GeneIDi855256.
KEGGisce:YMR216C.

Organism-specific databases

EuPathDBiFungiDB:YMR216C.
SGDiS000004829. SKY1.

Phylogenomic databases

GeneTreeiENSGT00530000063566.
HOGENOMiHOG000171558.
InParanoidiQ03656.
KOiK08832.
OMAiDASISCE.
OrthoDBiEOG7SV148.

Enzyme and pathway databases

BioCyciYEAST:G3O-32899-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ03656.
PROiQ03656.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 2 hits.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  4. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-383; SER-393; SER-449 AND SER-453, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  5. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-432; SER-445; SER-449 AND SER-453, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-383; THR-386; SER-388; SER-393; SER-410; SER-427; SER-432; SER-445; SER-449 AND SER-453, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "The structure of Sky1p reveals a novel mechanism for constitutive activity."
    Nolen B., Yun C.Y., Wong C.F., McCammon J.A., Fu X.-D., Ghosh G.
    Nat. Struct. Biol. 8:176-183(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 138-742, FUNCTION.
  8. "Nucleotide-induced conformational changes in the Saccharomyces cerevisiae SR protein kinase, Sky1p, revealed by X-ray crystallography."
    Nolen B., Ngo J., Chakrabarti S., Vu D., Adams J.A., Ghosh G.
    Biochemistry 42:9575-9585(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 138-742 ALONE AND IN COMPLEX WITH ADP AND ATP.

Entry informationi

Entry nameiSKY1_YEAST
AccessioniPrimary (citable) accession number: Q03656
Secondary accession number(s): D6W041
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 8, 2016
This is version 151 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2420 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.